8,945 research outputs found

    Constraints From Gauge Coupling Unification On The Scale Of Supersymmetry Breaking

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    We reanalyze precision LEP data and coupling constant unification in the minimal supersymmetric SU(5)SU(5) model including the evolution of the gaugino masses. We derive general bounds on the primordial gaugino supersymmetry-breaking mass-scale m1/2m_{1/2} in terms of the various input parameters. The model cannot accommodate m_{1/2}<1\TeV for values of \as < 0.115, even for extreme 1σ1-\sigma values of the other inputs. We emphasize the sensitivity of this type of calculations to the various input parameters.Comment: 9 pages, 1 figure not included, ACT-10/9

    Two-loop relation between the bare lattice coupling and the MSbar coupling in pure SU(N) gauge theories

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    We report the result of a computation of the relation between the renormalized coupling in the MSbar scheme of dimensional regularization and the bare coupling in the standard lattice formulation of the SU(N) Yang-Mills theory to two-loop order of perturbation theory and discuss some of its implications.Comment: 10 pages, postscript fil

    Proper Motion of the Faint Star near KIC 8462852 (Boyajian's Star) - Not a Binary System

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    A faint star located 2 arcsec from KIC 8462852 was discovered in Keck 10 m adaptive optics imaging in the JHKJHK near-infrared (NIR) in 2014 by Boyajian et al. (2016). The closeness of the star to KIC 8462852 suggested the two could constitute a binary, which might have implications for the cause of the brightness dips seen by {\it Kepler} (Boyajian et al. (2016) and in ground-based optical studies Boyajian et al. (2018). Here, NIR imaging in 2017 using the Mimir instrument resolved the pair and enabled measuring their separation. The faint star had moved 67±767 \pm 7 milliarcsec (mas) relative to KIC 8462852 since 2014. The relative proper motion of the faint star is 23.9±2.623.9 \pm 2.6 mas yr1^{-1}, for a tangential velocity of 45±545 \pm 5 km s1^{-1} if it is at the same 390 pc distance as KIC 8462852. Circular velocity at the 750 AU current projected separation is 1.51.5 km s1^{-1}, hence the star pair cannot be bound.Comment: 10 pages, 2 figure

    Matching the Low and High Energy Determinations of αs(Mz)\alpha_s(M_z) in the MSSM

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    Recent calculations of supersymmetric corrections to the conflicting ratios RbR_b and RcR_c have shown that an alleged discrepancy between the SM predictions of these observables and the corresponding experimental values can be cured in the MSSM within a certain region of the parameter space. Here we show that, in this very same region, also a well-known discrepancy between the low and high energy determinations of αs(MZ)\alpha_s(M_Z) can be disposed of. Specifically, we find that the lineshape determination of the strong coupling constant, which in the SM points towards the large central value αs(MZ)>0.125\alpha_s(M_Z) \stackrel{\scriptstyle >}{{ }_{\sim}} 0.125, can be matched up with the value suggested by the wealth of low-energy data, namely αs(MZ)0.11\alpha_s(M_Z) \simeq 0.11, which is smaller and more in line with the traditional QCD expectations at low energy. Our approach differs from previous analyses in that we argue that the desired matching could originate to a large extent from a purely electroweak supersymmetric quantum effect.Comment: 16 pages, LaTeX. Figures included and a few comments added. Full postscript version with figures embedded also available at ftp://ftp.ifae.es/preprint/ft/uabft365.p

    Paramyxovirus Glycoprotein Incorporation, Assembly and Budding: A Three Way Dance for Infectious Particle Production

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    Paramyxoviruses are a family of negative sense RNA viruses whose members cause serious diseases in humans, such as measles virus, mumps virus and respiratory syncytial virus; and in animals, such as Newcastle disease virus and rinderpest virus. Paramyxovirus particles form by assembly of the viral matrix protein, the ribonucleoprotein complex and the surface glycoproteins at the plasma membrane of infected cells and subsequent viral budding. Two major glycoproteins expressed on the viral envelope, the attachment protein and the fusion protein, promote attachment of the virus to host cells and subsequent virus-cell membrane fusion. Incorporation of the surface glycoproteins into infectious progeny particles requires coordinated interplay between the three viral structural components, driven primarily by the matrix protein. In this review, we discuss recent progress in understanding the contributions of the matrix protein and glycoproteins in driving paramyxovirus assembly and budding while focusing on the viral protein interactions underlying this process and the intracellular trafficking pathways for targeting viral components to assembly sites. Differences in the mechanisms of particle production among the different family members will be highlighted throughout

    Radiative Corrections to Neutralino and Chargino Masses in the Minimal Supersymmetric Model

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    We determine the neutralino and chargino masses in the MSSM at one-loop. We perform a Feynman diagram calculation in the on-shell renormalization scheme, including quark/squark and lepton/slepton loops. We find generically the corrections are of order 6%. For a 20 GeV neutralino the corrections can be larger than 20%. The corrections change the region of μ, M2, tanβ\mu,\ M_2,\ \tan\beta parameter space which is ruled out by LEP data. We demonstrate that, e.g., for a given μ\mu and tanβ\tan\beta the lower limit on the parameter M2M_2 can shift by 20 GeV.Comment: 11 pages, JHU-TIPAC-930030, PURD-TH-93-13, uses epsf.sty, 6 uuencoded postscript figures, added one sentence and a referenc

    Influence of Light and Heavy Thresholds on SUSY Unification

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    In this paper we study and compare susy unification using two different approaches in order to take into account the effect of light particle thresholds on the evolution of gauge couplings: the step--function approximation, on the one hand, and a mass dependent procedure, which gives a more accurate description of the dependence of the results on the masses, on the other. We also include the effect of heavy thresholds, when SU(5)SU(5) is chosen as the unifying group. We find that the mass--dependent procedure excludes scenarios where all susy masses are below 1  TeV1\;TeV, and favors a value of α3(mZ)\alpha_3(m_Z) near its upper experimental bound, contrary to the results obtained with the step--function approximation. We underline the dependence of the results on the procedure chosen to deal with light thresholds.Comment: 18 pages,LAEFF-93/014,REVTEX-2.1, 5 figures not included, available upon request (include FAX number)

    The Human Metapneumovirus Small Hydrophobic Protein has Properties Consistent with Those of a Viroporin and Can Modulate Viral Fusogenic Activity

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    Human metapneumovirus (HMPV) encodes three glycoproteins: the glycoprotein, which plays a role in glycosaminoglycan binding, the fusion (F) protein, which is necessary and sufficient for both viral binding to the target cell and fusion between the cellular plasma membrane and the viral membrane, and the small hydrophobic (SH) protein, whose function is unclear. The SH protein of the closely related respiratory syncytial virus has been suggested to function as a viroporin, as it forms oligomeric structures consistent with a pore and alters membrane permeability. Our analysis indicates that both the full-length HMPV SH protein and the isolated SH protein transmembrane domain can associate into higher-order oligomers. In addition, HMPV SH expression resulted in increases in permeability to hygromycin B and alteration of subcellular localization of a fluorescent dye, indicating that SH affects membrane permeability. These results suggest that the HMPV SH protein has several characteristics consistent with a putative viroporin. Interestingly, we also report that expression of the HMPV SH protein can significantly decrease HMPV F protein-promoted membrane fusion activity, with the SH extracellular domain and transmembrane domain playing a key role in this inhibition. These results suggest that the HMPV SH protein could regulate both membrane permeability and fusion protein function during viral infection. IMPORTANCE: Human metapneumovirus (HMPV), first identified in 2001, is a causative agent of severe respiratory tract disease worldwide. The small hydrophobic (SH) protein is one of three glycoproteins encoded by all strains of HMPV, but the function of the HMPV SH protein is unknown. We have determined that the HMPV SH protein can alter the permeability of cellular membranes, suggesting that HMPV SH is a member of a class of proteins termed viroporins, which modulate membrane permeability to facilitate critical steps in a viral life cycle. We also demonstrated that HMPV SH can inhibit the membrane fusion function of the HMPV fusion protein. This work suggests that the HMPV SH protein has several functions, though the steps in the HMPV life cycle impacted by these functions remain to be clarified
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